TY - JOUR
T1 - Lateral diffusion of GFP-tagged H2L(d) molecules and of GFP-TAP1 reports on the assembly and retention of these molecules in the endoplasmic reticulum
AU - Marguet, Didier
AU - Spiliotis, Elias T.
AU - Pentcheva, Tsvetelina
AU - Lebowitz, Michael
AU - Schneck, Jonathan
AU - Edidin, Michael
N1 - Funding Information:
We thank Drs. Marilyn Farquhar, Ted Hansen, André Lebivic, John Monaco, Luc Van Kaer, and Martha Zuniga for providing cells and reagents, Mrs. Taiyin Wei for expert technical support, and Mr. Andrew Nechkin of the Integrated Imaging Center, Department of Biology. This work was supported by National Institutes of Health grants AI14584 to M. E. and AI29575 to J. S. and by a grant from the National Multiple Sclerosis Foundation to J. S. (RG 2637A2/1). D. M. was supported in part by the Centre National de la Recherche Scientifique of France and by a fellowship from the North Atlantic Treaty Organization.
PY - 1999/8
Y1 - 1999/8
N2 - Lateral diffusion of GFP-tagged H2L(d) molecules in the ER membrane reports on their interaction with the TAP complex during synthesis and peptide loading. Peptide-loaded H2L(d) molecules diffuse rapidly, near the theoretical limit for proteins in a bilayer. However, these molecules are retained in the ER for some time after assembly. H2L(d) molecules, associated with the TAP complex, diffuse slowly, as does GFP-tagged TAP1. This implies that the association of H2L(d) molecules with the TAP complex is stable for at least several minutes. It also suggests that the TAP complex is very large, perhaps containing hundreds of proteins.
AB - Lateral diffusion of GFP-tagged H2L(d) molecules in the ER membrane reports on their interaction with the TAP complex during synthesis and peptide loading. Peptide-loaded H2L(d) molecules diffuse rapidly, near the theoretical limit for proteins in a bilayer. However, these molecules are retained in the ER for some time after assembly. H2L(d) molecules, associated with the TAP complex, diffuse slowly, as does GFP-tagged TAP1. This implies that the association of H2L(d) molecules with the TAP complex is stable for at least several minutes. It also suggests that the TAP complex is very large, perhaps containing hundreds of proteins.
UR - http://www.scopus.com/inward/record.url?scp=0033180470&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0033180470&partnerID=8YFLogxK
U2 - 10.1016/S1074-7613(00)80098-9
DO - 10.1016/S1074-7613(00)80098-9
M3 - Article
C2 - 10485658
AN - SCOPUS:0033180470
SN - 1074-7613
VL - 11
SP - 231
EP - 240
JO - Immunity
JF - Immunity
IS - 2
ER -